C1229
Monoclonal Anti-Caspase 10 antibody produced in rat
clone 25C2, purified immunoglobulin, buffered aqueous solution
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About This Item
Numer MDL:
Kod UNSPSC:
12352203
pochodzenie biologiczne
rat
białko sprzężone
unconjugated
forma przeciwciała
purified immunoglobulin
rodzaj przeciwciała
primary antibodies
klon
25C2, monoclonal
Postać
buffered aqueous solution
masa cząsteczkowa
antigen (full length) 59 kDa
antigen (subunit) 17 kDa
reaktywność gatunkowa
human
metody
microarray: suitable
western blot: 5-10 μg/mL using a whole extract of cultured human acute T cell leukemia Jurkat cells
izotyp
IgG2a
numer dostępu UniProt
Warunki transportu
dry ice
temp. przechowywania
−20°C
informacje o genach
human ... CASP10(843)
Opis ogólny
Caspases (Cysteine-requiring Aspartate protease) are a family of proteases that share similarities in amino acid sequences, structure and substrate specificity. Caspase-10 is an enzyme encoded by the CASP10 gene in humans. It is also known as Mch4, FLICE2 and ICE-LAP4 and encodes a “long” prodomain protein product of 59kDa (reported also as 55kDa). Four isoforms of caspase 10 (caspase 10a, 10b, 10c and 10d) have the same prodomain but different mature large and small subdomain. Caspase 10 undergoes a cleavage upon activation, leading to p17 and p12 subunits.
Immunogen
recombinant p17 subunit of human caspase-10.
Zastosowanie
Monoclonal Anti-Caspase 10 antibody produced in rat is suitable for microarray and western blotting at a concentration of 5-10μg/mL using a whole extract of cultured human acute T cell leukemia Jurkat cells.
Działania biochem./fizjol.
Caspase 10 is constitutively expressed in many fetal and adult tissues, with the lowest expression observed in brain, kidney, prostate, testis, and colon. Caspase 10 contains two death effector domains (DEDs) involved in the linking to the death effector domain of the adapter protein FADD and recruiting the complex to TNFR1 and Fas. Caspase 10 is one of the earliest caspases involved in the apoptosis induced cascade and may be responsible for the activation of most of the other caspases including caspase 3, 4, 6, 7 ,8 and 9.
Oświadczenie o zrzeczeniu się odpowiedzialności
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
T Fernandes-Alnemri et al.
Proceedings of the National Academy of Sciences of the United States of America, 93(15), 7464-7469 (1996-07-23)
Emerging evidence suggests that an amplifiable protease cascade consisting of multiple aspartate specific cysteine proteases (ASCPs) is responsible for the apoptotic changes observed in mammalian cells undergoing programmed cell death. Here we describe the cloning of two novel ASCPs from
R V Talanian et al.
The Journal of experimental medicine, 186(8), 1323-1331 (1997-10-23)
We report that the serine protease granzyme B (GrB), which is crucial for granule-mediated cell killing, initiates apoptosis in target cells by first maturing caspase-10. In addition, GrB has a limited capacity to mature other caspases and to cause cell
S M Srinivasula et al.
Proceedings of the National Academy of Sciences of the United States of America, 93(25), 14486-14491 (1996-12-10)
The Fas/APO-1-receptor associated cysteine protease Mch5 (MACH/FLICE) is believed to be the enzyme responsible for activating a protease cascade after Fas-receptor ligation, leading to cell death. The Fas-apoptotic pathway is potently inhibited by the cowpox serpin CrmA, suggesting that Mch5
G M Cohen
The Biochemical journal, 326 ( Pt 1), 1-16 (1997-08-15)
Apoptosis is a major form of cell death, characterized initially by a series of stereotypic morphological changes. In the nematode Caenorhabditis elegans, the gene ced-3 encodes a protein required for developmental cell death. Since the recognition that CED-3 has sequence
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